Regeneration of the photoprotein aequorin

@article{Shimomura1975RegenerationOT,
  title={Regeneration of the photoprotein aequorin},
  author={Osamu Shimomura and FRANK H. Johnson},
  journal={Nature},
  year={1975},
  volume={256},
  pages={236-238}
}
THE photoprotein aequorin (molecular weight about 30,000) isolated from the bioluminescent jellyfish Aequorea aequorea1–3 emits blue light (λm a x 470 nm)4 by an intramolecular reaction in aqueous solution when Ca2+ is added, in the presence or absence of molecular oxygen1. This reaction has been postulated5 to follow the scheme in (Fig. 1), in which an essential component H2O2 of aequorin is bound to the protein part in a form such as a peroxyacid or an α-hydroxyhydroperoxide which readily… 
The crystal structure of the photoprotein aequorin at 2.3 Å resolution
TLDR
The structure of recombinant aequorin is found to be a globular molecule containing a hydrophobic core cavity that accommodates the ligand coelenterazine-2-hydroperoxide and suggests a mechanism by which calcium activation may occur.
Uses and Physicochemical Properties of the Photoprotein Aequorin
The calcium-sensitive bioluminescent photoprotein aequorin is proving to be a useful tool for the measurement of [Ca2+] in living cells. Use of this protein has distinct advantages over other
THE ENZYMOLOGY AND MOLECULAR BIOLOGY OF THE Ca2+‐ACTIVATED PHOTOPROTEIN, AEQUORIN
TLDR
Comparisons of the coding regions of the two cDNAs show there are 52 nucleotide differences, 19 of which are responsible for 18 amino acid replacements, which explain the microheterogeneity observed at 17 positions during the sequencing of native apoaequorin.
Amino acid sequence of the calcium-dependent photoprotein aequorin.
TLDR
It is demonstrated that aequorin is a member of the Ca(II) binding protein superfamily and possesses three internally homologous domains which were judged to be EF-hand Ca( II) binding domains by several different criteria.
The discovery of aequorin and green fluorescent protein
TLDR
In the characterization of these proteins, information obtained from the bioluminescence of the ostracod Cypridina played an extremely important role, and without the information gained on CyPRidina luminescence, the characterize of aequorin would not have been possible.
The crystal structures of semi‐synthetic aequorins
TLDR
The differences of various semi‐synthetic aequorins in Ca2+‐sensitivity and reaction rate are explained by the capability of the involved groups and structures to undergo conformational changes in response to the Ca2+, particularly in the coelenterazine moiety.
...
...

References

SHOWING 1-10 OF 19 REFERENCES
Calcium Binding, Quantum Yield, and Emitting Molecule in Aequorin Bioluminescence
TLDR
The extreme sensitivity to Ca2+, much more than to Sr2+, provides a basis for quick microdetermination of Ca2+ in biological fluids and has been used in detecting the relation ofCa2+ to contraction of single muscle fibres and to activity of mitochondria.
Preparation and use of aequorin for rapid microdetermination of Ca 2+ in biological systems.
TLDR
The photoprotein aequorin extracted from the luminescent jellyfish Aequorea aequorea offers unique advantages for detecting the presence or changes in concentration of Ca2+ in biological systems and for investigating the action of poisons such as cyanide, tetrodotoxin and so on, on biological processes12–14.
Intermolecular energy transfer in the bioluminescent system of Aequorea.
TLDR
In the present study, GFP has been purified, crystallized, and partially characterized and an energy transfer in citro from aequorin to this protein has been demonstrated.
Chemical nature of bioluminescence systems in coelenterates.
  • O. ShimomuraF. Johnson
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 1975
Analysis of substances involved in light-emitting reactions among bioluminescent coelenterates has revealed a pronounced uniformity in the structural features of initial reactants, i.e., "luciferins"
Renilla luciferin as the substrate for calcium induced photoprotein bioluminescence. Assignment of luciferin tautomers in aequorin and mnemiopsin.
TLDR
The study of the effects of pH and protic and aprotic solvents on the spectral properties of Renilla (sea pansy) luciferin and a number of its analogs suggests that the native chromophore in both photoproteins is RenillaLuciferin (or a nearly identical derivative).
The "energized state" of mitochondria: lifetime and ATP equivalence.
Evidence for similar biochemical requirements for bioluminescence among the coelenterates
We present evidence that the chemical requirements among all the bioluminescent coelenterates that have been examined are very similar or identical to those already described for Renilla by Cormier
SQUID BIOLUMINESCENCE II. ISOLATION FROM WATASENIA SCINTILLANS AND SYNTHESIS OF 2-(p-HYDROXYBENZYL)-6-(p-HYDROXYPHENYL)-3,7-DIHYDROIMIDAZO[1,2-a]PYRAZIN-3-ONE
2-(p-Hydroxybenzyl)-6-(p-hydroxyphenyl)-3,7-dihydroimidazo[1,2-a]pyrazin-3-one was isolated from the squid, Watasenia scintillans. Its structure was determined by synthesis. It is considered to be a
Calcium influx in active Aplysia neurones detected by injected aequorin.
ACTION potentials may be recorded in Aplysia1,2 and Helix3 neurones in sodium and in calcium-free solutions, provided that either ion is present in the medium. The inward current may be due to both,
Calcium Transient in Presynaptic Terminal of Auid Giant Synapse: Detection with Aequorin
Microinjection of aequorin, a bioluminescent protein sensitive tocalcium, into the presynaptic terminal of the squid giant synapse demnonstrated an increase in intracellular calcium ion concentration
...
...